钙蛋白酶和组织蛋白酶B对肽基酰氧基甲基酮、锍甲基酮及其他半胱氨酸蛋白酶潜在抑制剂的比较行为
Comparative behaviour of calpain and cathepsin B toward peptidyl acyloxymethyl ketones, sulphonium methyl ketones and other potential inhibitors of cysteine proteinases.
作者信息
Pliura D H, Bonaventura B J, Smith R A, Coles P J, Krantz A
机构信息
Syntex Research, Mississauga, Ontario, Canada.
出版信息
Biochem J. 1992 Dec 15;288 ( Pt 3)(Pt 3):759-62. doi: 10.1042/bj2880759.
Abstract
Peptidyl acyloxymethyl ketones, previously established as potent inactivators of the lysosomal cysteine proteinase cathepsin B, were evaluated against smooth-muscle calpain, a member of the family of Ca(2+)-dependent cysteine proteinases. Only modest rates of time-dependent inhibition could be achieved, even with peptidyl affinity groups optimized for calpain and linked to a carboxylate leaving group of very low pKa [2,6-(CF3)2PhCOO-, pKa 0.58]. Selective inactivation of cathespin B versus calpain was consistently observed with this type of inhibitor. Examination of other potential inhibitors revealed a rank order of potency against calpain to be: peptidyl sulphonium methyl ketones > fluoromethyl ketones, diazomethyl ketones >> acyloxymethyl ketones, an order which differs sharply from that found for cathespin B.
摘要
肽基酰氧基甲基酮类化合物先前已被确认为溶酶体半胱氨酸蛋白酶组织蛋白酶B的有效失活剂，本研究对其针对平滑肌钙蛋白酶（一种依赖Ca(2+)的半胱氨酸蛋白酶家族成员）进行了评估。即使使用针对钙蛋白酶优化并与极低pKa的羧酸根离去基团[2,6-(CF3)2PhCOO-，pKa 0.58]相连的肽基亲和基团，也只能实现适度的时间依赖性抑制率。使用这类抑制剂时，始终观察到组织蛋白酶B相对于钙蛋白酶的选择性失活。对其他潜在抑制剂的研究表明，它们对钙蛋白酶的效力排序为：肽基锍甲基酮>氟甲基酮、重氮甲基酮>>酰氧基甲基酮，这一顺序与组织蛋白酶B的情况截然不同。
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本文引用的文献
1
Inactivation of thiol proteases with peptidyl diazomethyl ketones.用肽基重氮甲基酮使硫醇蛋白酶失活。
Methods Enzymol. 1981;80 Pt C:820-6. doi: 10.1016/s0076-6879(81)80064-x.
2
Inhibition of epoxide derivatives on chicken calcium-activated neutral protease (CANP) in vitro and in vivo.环氧化物衍生物在体外和体内对鸡钙激活中性蛋白酶（CANP）的抑制作用。
J Biochem. 1980 Jan;87(1):339-41. doi: 10.1093/oxfordjournals.jbchem.a132742.
3
An exploration of the primary specificity site of cathepsin B.组织蛋白酶B主要特异性位点的探索。
Arch Biochem Biophys. 1983 Apr 15;222(2):424-9. doi: 10.1016/0003-9861(83)90540-4.
4
Structure of papain refined at 1.65 A resolution.木瓜蛋白酶结构在1.65埃分辨率下的精修。
J Mol Biol. 1984 Oct 25;179(2):233-56. doi: 10.1016/0022-2836(84)90467-4.
5
Evolutionary origin of a calcium-dependent protease by fusion of genes for a thiol protease and a calcium-binding protein?一种钙依赖性蛋白酶是通过硫醇蛋白酶基因与钙结合蛋白基因融合而产生的进化起源？
Nature. 1984;312(5994):566-70. doi: 10.1038/312566a0.
6
Comparative specificity and kinetic studies on porcine calpain I and calpain II with naturally occurring peptides and synthetic fluorogenic substrates.
J Biol Chem. 1984 Oct 25;259(20):12489-94.
7
Synthesis of peptide fluoromethyl ketones and the inhibition of human cathepsin B.肽氟甲基酮的合成及对人组织蛋白酶B的抑制作用
Anal Biochem. 1985 Sep;149(2):461-5. doi: 10.1016/0003-2697(85)90598-6.
8
Peptidyl sulfonium salts. A new class of protease inhibitors.肽基锍盐。一类新型蛋白酶抑制剂。
J Biol Chem. 1988 Feb 25;263(6):2768-72.
9
Inhibition of cathepsin B by peptidyl aldehydes and ketones: slow-binding behavior of a trifluoromethyl ketone.
Biochemistry. 1988 Aug 23;27(17):6568-73. doi: 10.1021/bi00417a056.
10
Inactivation of calpain I and calpain II by specificity-oriented tripeptidyl chloromethyl ketones.通过特异性导向的三肽基氯甲基酮使钙蛋白酶I和钙蛋白酶II失活。
J Biochem. 1986 Jan;99(1):173-9. doi: 10.1093/oxfordjournals.jbchem.a135457.
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